Abstract
The structure of an N-terminal fragment of CD4 has been determined to 2.4 Å resolution. It has two tightly abutting domains connected by a continuous β strand. Both have the immunoglobulin fold, but domain 2 has a truncated β barrel and a non-standard disulphide bond. The binding sites for monoclonal antibodies, class II major histocom-patibility complex molecules, and human immunodeficiency virus gp120 can be mapped on the molecular surface.
Original language | English |
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Pages (from-to) | 411-418 |
Number of pages | 8 |
Journal | Nature |
Volume | 348 |
Issue number | 6300 |
DOIs | |
State | Published - 1990 |
Bibliographical note
Copyright:Copyright 2018 Elsevier B.V., All rights reserved.
ASJC Scopus subject areas
- General